Contribution of glycoproteins to fibrinogen-induced aggregation of erythrocytes.
The contribution of membrane glycoproteins to the velocity of fibrinogen-induced erythrocyte aggregation was examined using a rheoscope combined with a video camera, an image analyzer and a computer. The structure of glycoproteins was modified with proteolytic enzymes, trypsin or alpha-chymotrypsin. (1) Mild enzymatic treatment of erythrocytes decreased the velocity of erythrocyte aggregation, but more intense treatment increased the velocity remarkably. (2) The erythrocyte aggregation was affected not only by the density of surface negative charge of erythrocytes, but also by the structural changes of glycoproteins. (3) Erythrocyte deformability and the morphological characteristics were not altered by these enzymatic treatments. The physiological significance of glycoproteins of erythrocyte surface for the survival of erythrocytes and for the suspension stability of blood was discussed.
Maeda
N
N
Department of Physiology, School of Medicine, Ehime University, Japan.
Seike
M
M
Nakajima
T
T
Izumida
Y
Y
Sekiya
M
M
Shiga
T
T
D000328:Adult; D002241:Carbohydrates / Q000032:analysis; D002918:Chymotrypsin; D004903:Erythrocyte Aggregation / Q000187:drug effects*; D004907:Erythrocyte Deformability; D005340:Fibrinogen / Q000494:pharmacology*; D006801:Humans; D006868:Hydrolysis; D007202:Indicators and Reagents; D008297:Male; D008562:Membrane Glycoproteins / Q000378:metabolism*; D012794:Sialic Acids / Q000032:analysis; D014357:Trypsin
D002241:Carbohydrates; D007202:Indicators and Reagents; D008562:Membrane Glycoproteins; D012794:Sialic Acids; D005340:Fibrinogen; D002918:Chymotrypsin; D014357:Trypsin